title: Interaction of ladder-shaped polyethers with transmembrane alpha-helix of glycophorin A as evidenced by saturation transfer difference NMR and surface plasmon resonance.
abstract: Ladder-shaped polyether (LSP) compounds are thought to interact with transmembrane alpha-helices, but direct evidence has scarcely obtained for these interactions. We adopted a transmembrane alpha-helix of glycophorin A, and quantitatively evaluated its interaction with LSPs such as yessotoxin (YTX), desulfated YTX and artificial LSPs, using surface plasmon resonance and saturation transfer difference NMR. As a result, dissociation constants (K(D)) of YTX and desulfated YTX to a transmembrane domain peptide of glycophorin A were determined to be in the submillimolar range. Furthermore, in saturation transfer difference NMR, the signals at the polyene side chain and the angular methyl groups of YTX were significantly attenuated, which probably comprised an interacting interface of LSPs with a transmembrane alpha-helix. These results suggest that hydrophobic interaction plays an important role in molecular recognition of the alpha-helix peptide by LSPs.
authors.affiliation: Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
authors.forename: Satoru
authors.initials: S
authors.lastname: Ujihara
authors.forename: Tohru
authors.initials: T
authors.lastname: Oishi
authors.forename: Kohei
authors.initials: K
authors.lastname: Torikai
authors.forename: Keiichi
authors.initials: K
authors.lastname: Konoki
authors.forename: Nobuaki
authors.initials: N
authors.lastname: Matsumori
authors.forename: Michio
authors.initials: M
authors.lastname: Murata
authors.forename: Yasukatsu
authors.initials: Y
authors.lastname: Oshima
authors.forename: Saburo
authors.initials: S
authors.lastname: Aimoto
mesh_terms: D002922:Ciguatoxins / Q000737:chemistry; D004987:Ethers / Q000737:chemistry*; D006021:Glycophorins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008387:Marine Toxins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D008978:Mollusk Venoms; D035964:Oxocins / Q000737:chemistry; D011108:Polymers / Q000737:chemistry*; D013329:Structure-Activity Relationship; D000095702:Polyether Toxins
chemical_list: D002922:Ciguatoxins; D004987:Ethers; D006021:Glycophorins; D008387:Marine Toxins; D008565:Membrane Proteins; D008978:Mollusk Venoms; D035964:Oxocins; D011108:Polymers; C043466:brevetoxin B; D000095702:Polyether Toxins; C066632:yessotoxin